5jye
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structures of Streptococcus agalactiae GBS GAPDH in different enzymatic states== | |
| + | <StructureSection load='5jye' size='340' side='right' caption='[[5jye]], [[Resolution|resolution]] 2.23Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jye]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JYE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JYE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jyf|5jyf]], [[5jya|5jya]], [[5jy6|5jy6]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jye OCA], [http://pdbe.org/5jye PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jye RCSB], [http://www.ebi.ac.uk/pdbsum/5jye PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jye ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glyceraldehyde 3-phosphate dehydrogenase or GAPDH is an evolutionarily conserved glycolytic enzyme. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and NAD+ as cofactor. GAPDH of Group B Streptococcus is a major virulence factor and a potential vaccine candidate. Moreover, since GAPDH activity is essential for bacterial growth it may serve as a possible drug target. Crystal structures of Group B Streptococcus GAPDH in the apo-form, two different binary complexes and the ternary complex are described here. The two binary complexes contained NAD+ bound to 2 (mixed-holo) or 4 (holo) subunits of the tetrameric protein. The structure of the mixed-holo complex reveals the effects of NAD+ binding on the conformation of the protein. In the ternary complex, the phosphate group of the substrate was bound to the new Pi site in all four subunits. Comparison with the structure of human GAPDH showed several differences near the adenosyl binding pocket in Group B Streptococcus GAPDH. The structures also reveal at least three surface-exposed areas that differ in amino acid sequence compared to the corresponding areas of human GAPDH. | ||
| - | + | Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes.,Schormann N, Ayres CA, Fry A, Green TJ, Banerjee S, Ulett GC, Chattopadhyay D PLoS One. 2016 Nov 22;11(11):e0165917. doi: 10.1371/journal.pone.0165917., eCollection 2016. PMID:27875551<ref>PMID:27875551</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5jye" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Chattopadhyay, D]] | [[Category: Chattopadhyay, D]] | ||
[[Category: Schormann, N]] | [[Category: Schormann, N]] | ||
| + | [[Category: Gapdh]] | ||
| + | [[Category: Nad]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Rossmann fold]] | ||
Revision as of 21:32, 22 December 2016
Structures of Streptococcus agalactiae GBS GAPDH in different enzymatic states
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